Alanine dehydrogenase

alanine dehydrogenase
Identifiers
EC no.	1.4.1.1
CAS no.	9029-06-5
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

Alanine dehydrogenase (EC 1.4.1.1) is an enzyme that catalyzes the chemical reaction

alanine

+ NAD⁺

 

 

H₂O

H⁺

H₂O

H⁺

 

pyruvic acid

+ NADH + NH₃

 

The three substrates of this enzyme are alanine, water, and oxidised nicotinamide adenine dinucleotide (NAD⁺). Its products are pyruvic acid, reduced NADH, ammonia, and a proton. ^{[1] [2] [3]}

This enzyme participates in taurine and hypotaurine metabolism and reductive carboxylate cycle (CO₂ fixation). ^[1]

Nomenclature

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH₂ group of donors with NAD ⁺ or NADP ⁺ as acceptor. The systematic name of this enzyme class is L-alanine:NAD⁺ oxidoreductase (deaminating). Other names in common use include AlaDH, L-alanine dehydrogenase, NAD⁺-linked alanine dehydrogenase, alpha-alanine dehydrogenase, NAD⁺-dependent alanine dehydrogenase, alanine oxidoreductase, and NADH-dependent alanine dehydrogenase. T

Structure

Alanine dehydrogenase contains both a N-terminus ^[4] and C-terminus domains. ^{[5] [6]}

References

1. Enzyme 1.4.1.1 at KEGG Pathway Database.
2. O'Connor RJ, Halvorson H (March 1961). "The substrate specificity of L-alanine dehydrogenase". Biochimica et Biophysica Acta. 48 (1): 47–55. doi:10.1016/0006-3002(61)90513-3. PMID   13730044.
3. Yoshida A, Freese E (February 1965). "Enzymic properties of alanine dehydrogenase of Bacillus subtilis". Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation. 96 (2): 248–62. doi:10.1016/0926-6593(65)90009-3. PMID   14298830.
4. Pfam PF05222
5. Pfam PF01262
6. Tripathi SM, Ramachandran R (2008). "Crystal structures of the Mycobacterium tuberculosis secretory antigen alanine dehydrogenase (Rv2780) in apo and ternary complex forms captures "open" and "closed" enzyme conformations". Proteins. 72 (3): 1089–95. doi:10.1002/prot.22101. PMID   18491387. S2CID   23999004.